MYZAP_RAT
ID MYZAP_RAT Reviewed; 466 AA.
AC Q5EB94;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Myocardial zonula adherens protein;
DE Flags: Precursor;
GN Name=Myzap; Synonyms=Myozap;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP FUNCTION, INTERACTION WITH GRIN1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=18849881; DOI=10.1097/wnr.0b013e328317f05f;
RA Roginski R.S., Goubaeva F., Mikami M., Fried-Cassorla E., Nair M.R.,
RA Yang J.;
RT "GRINL1A colocalizes with N-methyl D-aspartate receptor NR1 subunit and
RT reduces N-methyl D-aspartate toxicity.";
RL NeuroReport 19:1721-1726(2008).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20093627; DOI=10.1161/circresaha.109.213256;
RA Seeger T.S., Frank D., Rohr C., Will R., Just S., Grund C., Lyon R.,
RA Luedde M., Koegl M., Sheikh F., Rottbauer W., Franke W.W., Katus H.A.,
RA Olson E.N., Frey N.;
RT "Myozap, a novel intercalated disc protein, activates serum response
RT factor-dependent signaling and is required to maintain cardiac function in
RT vivo.";
RL Circ. Res. 106:880-890(2010).
RN [4]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=29445566; DOI=10.5826/dpc.0801a01;
RA Abreu-Velez A.M., Gao W., Howard M.S.;
RT "Patients affected by endemic pemphigus foliaceus in Colombia, South
RT America exhibit autoantibodies to optic nerve sheath envelope cell
RT junctions.";
RL Dermatol. Pract. Concept. 8:1-6(2018).
RN [5]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=31384490; DOI=10.5826/dpc.0903a02;
RA Abreu-Velez A.M., Upegui-Zapata Y.A., Valencia-Yepes C.A.,
RA Upegui-Quiceno E., Jimenez-Echavarria A.M., Nino-Pulido C.D., Smoller B.R.,
RA Howard M.S.;
RT "Involvement of the Areae Compositae of the Heart in Endemic Pemphigus
RT Foliaceus.";
RL Dermatol. Pract. Concept. 9:181-186(2019).
CC -!- FUNCTION: Plays a role in cellular signaling via Rho-related GTP-
CC binding proteins and activation of transcription factor SRF. Targets
CC TJP1 to cell junctions (By similarity). In cortical neurons, may play a
CC role in glutaminergic signal transduction through interaction with the
CC NMDA receptor subunit GRIN1. {ECO:0000250,
CC ECO:0000269|PubMed:18849881}.
CC -!- SUBUNIT: Interacts with DSP, MPRIP and TJP1/ZO1. Interaction with MPRIP
CC inhibits the activation of transcription factor SRF (By similarity).
CC Interacts with GRIN1. Interacts with DYNLL1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:20093627}. Cell membrane
CC {ECO:0000269|PubMed:18849881, ECO:0000269|PubMed:20093627}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:Q3UIJ9}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q3UIJ9}. Cytoplasm, myofibril, sarcomere, I band
CC {ECO:0000250|UniProtKB:Q3UIJ9}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250|UniProtKB:Q3UIJ9}. Cell junction
CC {ECO:0000269|PubMed:29445566, ECO:0000269|PubMed:31384490}.
CC Note=Detected predominantly at the intercalated disk in cardiomyocytes,
CC and at low levels on sarcomeric Z disKs. Colocalizes with F-actin.
CC Colocalizes with cortical actin (PubMed:20093627). In neurons,
CC colocalizes with GRIN1 in postsynaptic neurites (PubMed:18849881). In
CC heart, localizes at area composita, the mixed-type junctional structure
CC composed of both desmosomal and adherens junctional proteins
CC (PubMed:31384490). {ECO:0000269|PubMed:18849881,
CC ECO:0000269|PubMed:20093627, ECO:0000269|PubMed:31384490}.
CC -!- TISSUE SPECIFICITY: Detected in brain, heart and lung (at protein
CC level) (PubMed:31384490). Expressed in optic nerve sheath envelope(at
CC protein level) (PubMed:29445566). {ECO:0000269|PubMed:18849881,
CC ECO:0000269|PubMed:20093627, ECO:0000269|PubMed:29445566,
CC ECO:0000269|PubMed:31384490}.
CC -!- SIMILARITY: Belongs to the MYZAP family. {ECO:0000305}.
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DR EMBL; BC089899; AAH89899.1; -; mRNA.
DR RefSeq; NP_001014233.1; NM_001014211.1.
DR AlphaFoldDB; Q5EB94; -.
DR SMR; Q5EB94; -.
DR BioGRID; 263959; 1.
DR STRING; 10116.ENSRNOP00000023153; -.
DR CarbonylDB; Q5EB94; -.
DR iPTMnet; Q5EB94; -.
DR PhosphoSitePlus; Q5EB94; -.
DR PRIDE; Q5EB94; -.
DR Ensembl; ENSRNOT00000077999; ENSRNOP00000075263; ENSRNOG00000057676.
DR GeneID; 363091; -.
DR KEGG; rno:363091; -.
DR UCSC; RGD:1359197; rat.
DR CTD; 100820829; -.
DR RGD; 1359197; Myzap.
DR eggNOG; ENOG502QSEE; Eukaryota.
DR GeneTree; ENSGT00950000183065; -.
DR HOGENOM; CLU_022112_0_0_1; -.
DR InParanoid; Q5EB94; -.
DR OrthoDB; 639997at2759; -.
DR PhylomeDB; Q5EB94; -.
DR TreeFam; TF331627; -.
DR PRO; PR:Q5EB94; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000057676; Expressed in heart and 20 other tissues.
DR ExpressionAtlas; Q5EB94; baseline and differential.
DR Genevisible; Q5EB94; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0031674; C:I band; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR InterPro; IPR028273; Myozap.
DR PANTHER; PTHR23171:SF2; PTHR23171:SF2; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..466
FT /note="Myocardial zonula adherens protein"
FT /id="PRO_0000326227"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 95..137
FT /evidence="ECO:0000255"
FT COILED 180..415
FT /evidence="ECO:0000255"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 466 AA; 53955 MW; F359D740C2B91543 CRC64;
MLRSTSTVTL LSGGSAKSPG TPSRRANVCR LRLTVPPENP VPQQKEKKIE RKDQPPELSN
GESTKKLPQG VVYGVVRRSD PNQQKEMVVY GWSTNQLKEE MNYIKDVRAT LEKVRKRMYG
DYDEMRQKIR QLTQDLSVSH AQQDYLDSHI QAQASALDSF NAMNSALALD SVGLQKTLVD
VTLENSNIKD QIRHLQQTYE ASMDKLREKQ RQLEAAQMEN QLLKMRVESS QEANAEVMRE
MTRKLYSQYE EKLQEAQRKH SAEKEVLLEE TNSFLKAIEE ANKKMEAAEL SLEEKDQRIG
ELDRLIERME KERHQLQLQL LEHETEMSGE MADFDKNRYQ QLEEASASLR ERIRHLDDMV
HCQQKKVKQM VEEIESLKKK VQQKQLLILQ LLEKISFLEG ENNELQSRLD YLTETQPKTE
VETREIGVGC DLLPSTTGRT REIAVPSRSY TPYTRVLELT SKKTLT
